Phospho-STAT1 (Ser727)抗体;Phospho-STAT1 (Ser727) Antibody—艾普蒂 新品

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     Western blot analysis of Phospho-STAT1 (S727) in HeLa lysates treated with etoposide using Phospho-STAT1 (Ser727) antibody.    

  
  

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     Immunohistochemistry analysis of paraffin-embedded Human lung cancer using Phospho-STAT1 (S727) antibody.High-pressure and temperature Sodium Citrate pH 6.0 was used for antigen retrieval.    

  
  

Phospho-STAT1 (Ser727) antibody is a key tool for studying the activation and regulation of Signal Transducer and Activator of Transcription 1 (STAT1), a transcription factor critical in mediating cellular responses to cytokines, growth factors, and interferons (IFNs). STAT1 is activated through phosphorylation at two primary sites: tyrosine 701 (Tyr701) and serine 727 (Ser727). Phosphorylation at Tyr701. mediated by Janus kinases (JAKs) or receptor tyrosine kinases, induces STAT1 dimerization, nuclear translocation, and DNA binding. In contrast, Ser727 phosphorylation occurs in the transactivation domain and is mediated by kinases such as mTOR, p38 MAPK, or CAMKII, enhancing transcriptional activity by promoting interactions with coactivators like p300/CBP. This post-translational modification also links STAT1 to non-canonical roles, including mitochondrial function and apoptosis regulation.

Phospho-STAT1 (Ser727)-specific antibodies enable researchers to detect and quantify STAT1 activation at this site using techniques like Western blotting, immunofluorescence, or flow cytometry. These antibodies are widely used to study immune responses, viral infections, and cancer, where dysregulated STAT1 signaling contributes to pathogenesis. For example, they help assess STAT1 activation in IFN-treated cells, autoimmune disorders, or tumors with constitutively active signaling pathways. Proper experimental controls (e.g., unphosphorylated STAT1 detection and kinase inhibition) are essential to confirm specificity. Understanding Ser727 phosphorylation provides insights into the nuanced regulation of STAT1-dependent gene expression and its broader cellular roles.